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AA-Amyloid is cleared by endogenous immunological mechanisms
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology.
2012 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 19, no 3, 138-145 p.Article in journal (Refereed) Published
Abstract [en]

Objective: AA amyloidosis is a complication to longstanding inflammatory diseases, but reduction of amyloid mass has been reported as the inflammation ceases. Not much is known about the endogenous factors that contribute to this amyloid resolution. Herein, we describe the dynamics of amyloid degradation and resolution in experimental murine AA-amyloidosis.

Methods: AA-amyloidosis was induced in mice with injections of amyloid enhancing factor (AEF) and by inflammation induced with injections of silver nitrate. Resolution of amyloid deposits was monitored over time.

Results: Virtually all amyloid was cleared within 34 weeks. Using the ELISA-technique, antibodies directed against protein AA were detected in animals during amyloid clearance phase and macrophages were shown to internalize amyloid. Also, passive immunization with an amyloid specific monoclonal antibody, produced by a B-cell clone recovered from an animal with advanced AA-amyloidosis, reduced amyloid development in murine AA-amyloidosis.

Conclusion: Immunoglobulins co-localize with amyloid deposits and can contribute to amyloid degradation by Fc-receptor mediated phagocytosis, and should be considered key players in the degradation process.

Place, publisher, year, edition, pages
2012. Vol. 19, no 3, 138-145 p.
Keyword [en]
AA-amyloid, antibodies, macrophages, mice, resolution
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-181834DOI: 10.3109/13506129.2012.711391ISI: 000307635600004OAI: oai:DiVA.org:uu-181834DiVA: diva2:558146
Available from: 2012-10-02 Created: 2012-10-01 Last updated: 2017-12-07Bibliographically approved

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Westermark, Gunilla T.

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